Porphyromonas gingivalis ProteaseによるKallikrein-Kinin Cascadeの活性化
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概要
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A thiol-activatable protease which had been isolated from a culture supernatant of Porphyromonas gingivalis, a putative periodontal pathogen, caused vascular permeability enhacement in a dose dependent manner when injected into guinea pig skin. The enhancement reaction was not affected by antihistamine, the involvement of the bradykinin-generating system in this permeability enhancement was investigatd. The permeability enhancing reaction of the protease was inhibited by soybean trypsin inhibitor, a well known inhibitor of plasma kallikrein, and also by α _2-antiplasmin, which inhibits both plasma kallikrein and plasmin. However, the reaction was not affected by a corn trypsin inhibitor, which is the best inhibitor of the activated Hageman factor. In vitro experiments using the synthetic substrate, Z-phe-arg-MCA ; a specific substrate for plasma kallikrein, the protease cleaved it as did kallikrein in a dose dependent manner and an increase of 7-amino- 4-methylcoumarin release was observed. The enhancement reaction by the protease was greatly augmented by the kinin potentiator, carboxypeptidase N inhibitor, but was reduced apparently by the kinin-degrading enzyme, carboxypeptidase B, suggesting the generation of bradykinin. The results of this study indicate that the permeability enhancing reaction induced by P. gingivalis protease is caused by activation of the kallikrein kinin cascade in the tissue.
- 福岡歯科大学学会の論文
- 1995-03-31